Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (A/Bellamy/1942(H1N1))
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalytic activityi

Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.UniRule annotationSAAS annotation

Cofactori

Ca2+UniRule annotationSAAS annotation

Activity regulationi

Inhibited by the neuraminidase inhibitors zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere with the release of progeny virus from infected cells and are effective against all influenza strains. Resistance to neuraminidase inhibitors is quite rare.SAAS annotation

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidaseUniRule annotationSAAS annotation, Hydrolase
LigandCalciumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
NeuraminidaseUniRule annotationSAAS annotation (EC:3.2.1.18UniRule annotationSAAS annotation)
Gene namesi
Name:NAUniRule annotationImported
OrganismiInfluenza A virus (A/Bellamy/1942(H1N1))Imported
Taxonomic identifieri384529 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeAlphainfluenzavirus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei7 – 34HelicalSequence analysisAdd BLAST28

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membraneUniRule annotationSAAS annotation, Host membrane, Membrane, VirionUniRule annotationSAAS annotation

PTM / Processingi

Post-translational modificationi

N-glycosylated.UniRule annotation

Keywords - PTMi

Disulfide bondSAAS annotation, GlycoproteinUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotationSAAS annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 34 family.UniRule annotationSAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysisSAAS annotation

Family and domain databases

InterProiView protein in InterPro
IPR001860 Glyco_hydro_34
IPR036278 Sialidase_sf
PfamiView protein in Pfam
PF00064 Neur, 1 hit
SUPFAMiSSF50939 SSF50939, 1 hit

Sequencei

Sequence statusi: Fragment.

E0AGJ0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNPNQKIITI GSICMVVGII SLILQIGNII SIWISHSIQT GSQNHTGICN
60 70 80 90 100
QSIITYKNST WVNQTYVNIS NTNVVAGKDT TSMILAGNSS LCPIRGWAIY
110 120 130 140 150
SKDNGIRIGS KGDVFVIREP FISCSHLECR TFFLTQGALL NDKHSNGTVK
160 170 180 190 200
DRSPYRALMS CPVGEAPSPY NSRFESVAWS ASACHDGMGW LTIGISGPDD
210 220 230 240
GAVAVLKYNG IITETIKSWK KKILRTQESE CVCVNGSCFT IMTDGP
Length:246
Mass (Da):26,716
Last modified:October 5, 2010 - v1
Checksum:iA46CF38F528331A1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei246Imported1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ008262 Viral cRNA Translation: ADK95052.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ008262 Viral cRNA Translation: ADK95052.1

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiView protein in InterPro
IPR001860 Glyco_hydro_34
IPR036278 Sialidase_sf
PfamiView protein in Pfam
PF00064 Neur, 1 hit
SUPFAMiSSF50939 SSF50939, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiE0AGJ0_9INFA
AccessioniPrimary (citable) accession number: E0AGJ0
Entry historyiIntegrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: October 10, 2018
This is version 33 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again